A lysine rich C-terminal tail is directly involved in the toxicity of CSTX-1, a neurotoxic peptide from the venom of the spider Cupiennius salei

Archives of Insect Biochemistry and Physiology

Volumn 44, Issue 3, 2000, Pages 101-111

  Kuhn Nentwig, Lucia ^a   Schaller, Johann ^a   Kämpfer, Urs ^a   Imboden, Hans ^a   Malli, Heinz ^a   Nentwig, Wolfgang ^a  

^a UNIVERSITY OF BERN   (Switzerland)

Author keywords

Amino acid sequence; Apocrine secretion; CSTX 2a; CSTX 2b; LD50; Proteolytic activity; Spider toxin CSTX 1

Indexed keywords

AMINO ACID; BLOOD CLOTTING FACTOR 10A; CSTX 2A PROTEIN, CUPIENNIUS SALEI; CSTX-2A PROTEIN, CUPIENNIUS SALEI; ENTEROPEPTIDASE; LYSINE; NEUROTOXIN; PEPTIDE; PROTEINASE; REPTILIAN PROTEIN; SPIDER VENOM;

AMINO ACID SEQUENCE; ANIMAL; ARTICLE; BINDING SITE; BIOASSAY; CHEMISTRY; DROSOPHILA MELANOGASTER; ISOLATION AND PURIFICATION; METABOLISM; METHODOLOGY; MOLECULAR GENETICS; SEQUENCE ANALYSIS; SPIDER;

AMINO ACID SEQUENCE; AMINO ACIDS; ANIMALS; BINDING SITES; BIOLOGICAL ASSAY; DROSOPHILA MELANOGASTER; ENDOPEPTIDASES; ENTEROPEPTIDASE; FACTOR XA; LYSINE; MOLECULAR SEQUENCE DATA; NEUROTOXINS; PEPTIDES; REPTILIAN PROTEINS; SEQUENCE ANALYSIS; SPIDER VENOMS; SPIDERS;

EID: 0034218788     PISSN: 07394462     EISSN: None     Source Type: Journal    
DOI: 10.1002/1520-6327(200007)44:3<101::AID-ARCH1>3.0.CO;2-S     Document Type: Article

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